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Conserved domains on  [gi|119605959|gb|EAW85553|]
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polycystic kidney disease 1 (autosomal dominant), isoform CRA_a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
97-2728 0e+00

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 4862.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959    97 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLAWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSGC 176
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   177 GEEYVACLPDNSSGTVAAVS----FSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFACLSLCSGPP 252
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   253 PPPAPTCRGPTLLQHVFPASPGATLVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSAEVDAAGP----AASHRYVLP 328
Cdd:TIGR00864  161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   329 GRYHVTAVLALGAGSALLGTDVQVEAAPAALELVCPSSVQSDESLDLSIQNRGGSGLEAAYSIVALGEEPARAVHPLCPS 408
Cdd:TIGR00864  241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   409 DTEIFPGNGHCYRLVVEKAAWLQAQEQCQAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGVEVGPAPQGEA 486
Cdd:TIGR00864  321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   487 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLAQQDGL 566
Cdd:TIGR00864  401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   567 SAP-HEPVEVMVFPGLRLSREAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLAPACMP 642
Cdd:TIGR00864  481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   643 GGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAP----YALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864  561 GEQWCPFAHICLPLDAPCHPQACANGCSQGHGLPGAArmplYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   719 HDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPH------------------------LPAQLEGTWA----CPACALR 770
Cdd:TIGR00864  641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRAswleCAACAIR 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFDVVSPVAGLRVIYPAPRDGRLYVPTNGSALVLQVD 850
Cdd:TIGR00864  721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   851 SGANATATARWPGGSVSARFENVCPALVA-------TFVPGCPWETNDTLFSVVALPWLSEGEHV----VDVVVENSASR 919
Cdd:TIGR00864  801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTAS 999
Cdd:TIGR00864  881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAM 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1000 NHVSNVTVNYNVTVERMNRMQGLQVSTVPAVLSPNATLALTAGVLVDSAVEVAFLWTFGDGEQALHQFQPPYNESFPVPD 1079
Cdd:TIGR00864  961 NHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1080 PSVAQVLVEHNVMHTYAAPGEYLLTVLASNAFENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLY 1159
Cdd:TIGR00864 1041 PSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1160 TWDFGDGSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDMSLAVEQGAPVVVSAAVQTGD 1239
Cdd:TIGR00864 1121 EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGD 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1240 NITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTG 1319
Cdd:TIGR00864 1201 NITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSG 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1320 NPAHYLFDWTFGDGSSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVTLQPERQFVQLGDEAW 1399
Cdd:TIGR00864 1281 NAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQ 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1400 LVACAWPPFPYRYTWDFGTEEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQEPVLVTSIKVNGSLG- 1478
Cdd:TIGR00864 1361 FQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHGn 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1479 -LELQQPYLFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASR 1557
Cdd:TIGR00864 1441 nLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASL 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1558 TVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQV 1637
Cdd:TIGR00864 1521 TNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQI 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1638 VGG-------------GRYFPTNHTVQLQAVVRDGTNVSYSWTAWRD---RGPALAGSGKGFSLTVLEAGTYHVQLRATN 1701
Cdd:TIGR00864 1601 LGEtaegggggvqeldGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN 1680
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1702 MLGSAWADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTM 1781
Cdd:TIGR00864 1681 LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTM 1760
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1782 TAGNPLGSANATVEVDVQVPVSGLSIRASEPGGS-FVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAG 1860
Cdd:TIGR00864 1761 KAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAG 1840
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1861 TFSIRLNASNAVSWVSATYNLTAEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVL-PGPRFSHS 1939
Cdd:TIGR00864 1841 TFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHS 1920
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1940 FPRVGDHVVSVRGKNHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLV 2019
Cdd:TIGR00864 1921 FPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLV 2000
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2020 ILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALQSGP--CFTNRSAQFEAATSPSPRRVAYHWDFG 2097
Cdd:TIGR00864 2001 IHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFG 2080
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2098 DGSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRD 2177
Cdd:TIGR00864 2081 DGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKD 2160
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2178 CVTYQTEYRWEVYRTASCQRPGRPARVALPG-------------VDVSRPRLVLPRLALPVGHYCFVFVVSFGDTPLTQS 2244
Cdd:TIGR00864 2161 CLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA 2240
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2245 IQANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSTV 2323
Cdd:TIGR00864 2241 ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTL 2320
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2324 TIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRG 2403
Cdd:TIGR00864 2321 GIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRG 2400
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2404 RWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRPPLGGSCRLFPLG- 2482
Cdd:TIGR00864 2401 RWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGe 2480
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2483 -------------AVHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFE 2548
Cdd:TIGR00864 2481 tgqehgdkedevwAIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFE 2560
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2549 VGLAVVVQDQLGAAVVALNRSLAITLPEPNGSATGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYERALDV 2628
Cdd:TIGR00864 2561 VGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDS 2640
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2629 AAEPKHERQHRAQIRKNITETLVSLRVHTVDDIQQIAAALAQCMGPSRELVCRSCLKQTLHKLEAMMLILQAETTAGTVT 2708
Cdd:TIGR00864 2641 AAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVT 2720
                         2730      2740
                   ....*....|....*....|
gi 119605959  2709 PTAIGDSILNITGDLIHLAS 2728
Cdd:TIGR00864 2721 PTAIADNILNIMGDLIHLAS 2740
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
3118-3237 8.80e-58

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238850  Cd Length: 120  Bit Score: 196.34  E-value: 8.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAW 3195
Cdd:cd01752     1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119605959 3196 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLAA 3237
Cdd:cd01752    81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom super family cl48672
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3713-3891 5.05e-56

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


The actual alignment was detected with superfamily member pfam20519:

Pssm-ID: 466668  Cd Length: 199  Bit Score: 194.56  E-value: 5.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3713 AFLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEA--LYPDPPGPRVHTCSAAGGFST 3778
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSscLVHDKFVREINECHAGYSPPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3779 SDY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDNRSRAVFL 3852
Cdd:pfam20519   81 EDRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119605959  3853 ELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3891
Cdd:pfam20519  161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel super family cl37568
Polycystin cation channel; This family contains the cation channel region from group II of ...
3892-4113 6.81e-44

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


The actual alignment was detected with superfamily member pfam08016:

Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 160.91  E-value: 6.81e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3892 RLSAGLSLPLLT-SVCLLLFAVHFAVAEARTWHREGR------WRVLRLgawarwLLVALTAATALVRLAQLGAADRQWT 3964
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRPsylrsvWNLLDL------AIVILSVVLIVLNIYRDFLADRLIK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3965 rFVRGRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLA 4044
Cdd:pfam08016   75 -SVEASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFG 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959  4045 ILLVSSCVDSLWSVAQALLVLCPgtglsTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4113
Cdd:pfam08016  154 YLLFGTQAPNFSNFVKSILTLFR-----TILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
GPS super family cl02559
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
3011-3060 3.22e-10

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


The actual alignment was detected with superfamily member smart00303:

Pssm-ID: 470616  Cd Length: 49  Bit Score: 58.17  E-value: 3.22e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 119605959   3011 YTSLCQYFSEEDMVWRTEGLLPLEETSpRQAVCLTRHLTAFGASLFVPPS 3060
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFAVLMDVPPI 49
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
54-127 6.35e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd21340:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 220  Bit Score: 59.41  E-value: 6.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959   54 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSALAELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 127
Cdd:cd21340   113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
 
Name Accession Description Interval E-value
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
97-2728 0e+00

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 4862.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959    97 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLAWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSGC 176
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   177 GEEYVACLPDNSSGTVAAVS----FSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFACLSLCSGPP 252
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   253 PPPAPTCRGPTLLQHVFPASPGATLVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSAEVDAAGP----AASHRYVLP 328
Cdd:TIGR00864  161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   329 GRYHVTAVLALGAGSALLGTDVQVEAAPAALELVCPSSVQSDESLDLSIQNRGGSGLEAAYSIVALGEEPARAVHPLCPS 408
Cdd:TIGR00864  241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   409 DTEIFPGNGHCYRLVVEKAAWLQAQEQCQAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGVEVGPAPQGEA 486
Cdd:TIGR00864  321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   487 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLAQQDGL 566
Cdd:TIGR00864  401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   567 SAP-HEPVEVMVFPGLRLSREAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLAPACMP 642
Cdd:TIGR00864  481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   643 GGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAP----YALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864  561 GEQWCPFAHICLPLDAPCHPQACANGCSQGHGLPGAArmplYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   719 HDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPH------------------------LPAQLEGTWA----CPACALR 770
Cdd:TIGR00864  641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRAswleCAACAIR 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFDVVSPVAGLRVIYPAPRDGRLYVPTNGSALVLQVD 850
Cdd:TIGR00864  721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   851 SGANATATARWPGGSVSARFENVCPALVA-------TFVPGCPWETNDTLFSVVALPWLSEGEHV----VDVVVENSASR 919
Cdd:TIGR00864  801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTAS 999
Cdd:TIGR00864  881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAM 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1000 NHVSNVTVNYNVTVERMNRMQGLQVSTVPAVLSPNATLALTAGVLVDSAVEVAFLWTFGDGEQALHQFQPPYNESFPVPD 1079
Cdd:TIGR00864  961 NHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1080 PSVAQVLVEHNVMHTYAAPGEYLLTVLASNAFENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLY 1159
Cdd:TIGR00864 1041 PSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1160 TWDFGDGSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDMSLAVEQGAPVVVSAAVQTGD 1239
Cdd:TIGR00864 1121 EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGD 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1240 NITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTG 1319
Cdd:TIGR00864 1201 NITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSG 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1320 NPAHYLFDWTFGDGSSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVTLQPERQFVQLGDEAW 1399
Cdd:TIGR00864 1281 NAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQ 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1400 LVACAWPPFPYRYTWDFGTEEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQEPVLVTSIKVNGSLG- 1478
Cdd:TIGR00864 1361 FQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHGn 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1479 -LELQQPYLFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASR 1557
Cdd:TIGR00864 1441 nLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASL 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1558 TVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQV 1637
Cdd:TIGR00864 1521 TNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQI 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1638 VGG-------------GRYFPTNHTVQLQAVVRDGTNVSYSWTAWRD---RGPALAGSGKGFSLTVLEAGTYHVQLRATN 1701
Cdd:TIGR00864 1601 LGEtaegggggvqeldGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN 1680
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1702 MLGSAWADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTM 1781
Cdd:TIGR00864 1681 LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTM 1760
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1782 TAGNPLGSANATVEVDVQVPVSGLSIRASEPGGS-FVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAG 1860
Cdd:TIGR00864 1761 KAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAG 1840
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1861 TFSIRLNASNAVSWVSATYNLTAEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVL-PGPRFSHS 1939
Cdd:TIGR00864 1841 TFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHS 1920
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1940 FPRVGDHVVSVRGKNHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLV 2019
Cdd:TIGR00864 1921 FPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLV 2000
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2020 ILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALQSGP--CFTNRSAQFEAATSPSPRRVAYHWDFG 2097
Cdd:TIGR00864 2001 IHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFG 2080
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2098 DGSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRD 2177
Cdd:TIGR00864 2081 DGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKD 2160
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2178 CVTYQTEYRWEVYRTASCQRPGRPARVALPG-------------VDVSRPRLVLPRLALPVGHYCFVFVVSFGDTPLTQS 2244
Cdd:TIGR00864 2161 CLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA 2240
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2245 IQANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSTV 2323
Cdd:TIGR00864 2241 ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTL 2320
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2324 TIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRG 2403
Cdd:TIGR00864 2321 GIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRG 2400
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2404 RWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRPPLGGSCRLFPLG- 2482
Cdd:TIGR00864 2401 RWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGe 2480
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2483 -------------AVHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFE 2548
Cdd:TIGR00864 2481 tgqehgdkedevwAIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFE 2560
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2549 VGLAVVVQDQLGAAVVALNRSLAITLPEPNGSATGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYERALDV 2628
Cdd:TIGR00864 2561 VGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDS 2640
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2629 AAEPKHERQHRAQIRKNITETLVSLRVHTVDDIQQIAAALAQCMGPSRELVCRSCLKQTLHKLEAMMLILQAETTAGTVT 2708
Cdd:TIGR00864 2641 AAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVT 2720
                         2730      2740
                   ....*....|....*....|
gi 119605959  2709 PTAIGDSILNITGDLIHLAS 2728
Cdd:TIGR00864 2721 PTAIADNILNIMGDLIHLAS 2740
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
2171-2614 7.84e-133

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 425.76  E-value: 7.84e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2171 AHVDLRDCV-TYQTEYRWEVYRTASC---QRPGRPARVALPGVDvsrprlvLPRLALPVGHYCFVFVVSFGDTP-LTQSI 2245
Cdd:pfam02010    1 ASVELNGCFsAYTIDYLWSVFTVSSNlnlQTISSPKDLVLPQLT-------IPSGTLPYGTYVFTLTVSLSSTPsLAGTD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2246 QANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LN 2314
Cdd:pfam02010   74 IITVTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2315 FGPRGSSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCL 2394
Cdd:pfam02010  154 LLQSTSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2395 NCSSGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRP 2470
Cdd:pfam02010  232 NCSSDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAP 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2471 PLGGSCRLFPLGAvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FE 2548
Cdd:pfam02010  312 PTGGTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQ 387
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959  2549 VGLAVVVQDQLGAAvVALNRSLAITLPEPNGSatglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2614
Cdd:pfam02010  388 VTVVVVVYDSLGAA-TSVSLTITVTPPSSSDE----LLYFLLGTTSDLSALLQSGDPQQAAQLILA 448
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
3118-3237 8.80e-58

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 196.34  E-value: 8.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAW 3195
Cdd:cd01752     1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119605959 3196 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLAA 3237
Cdd:cd01752    81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3713-3891 5.05e-56

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 194.56  E-value: 5.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3713 AFLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEA--LYPDPPGPRVHTCSAAGGFST 3778
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSscLVHDKFVREINECHAGYSPPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3779 SDY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDNRSRAVFL 3852
Cdd:pfam20519   81 EDRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119605959  3853 ELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3891
Cdd:pfam20519  161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
3892-4113 6.81e-44

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 160.91  E-value: 6.81e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3892 RLSAGLSLPLLT-SVCLLLFAVHFAVAEARTWHREGR------WRVLRLgawarwLLVALTAATALVRLAQLGAADRQWT 3964
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRPsylrsvWNLLDL------AIVILSVVLIVLNIYRDFLADRLIK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3965 rFVRGRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLA 4044
Cdd:pfam08016   75 -SVEASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFG 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959  4045 ILLVSSCVDSLWSVAQALLVLCPgtglsTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4113
Cdd:pfam08016  154 YLLFGTQAPNFSNFVKSILTLFR-----TILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
WSC smart00321
present in yeast cell wall integrity and stress response component proteins; Domain present in ...
177-271 2.95e-24

present in yeast cell wall integrity and stress response component proteins; Domain present in WSC proteins, polycystin and fungal exoglucanase


Pssm-ID: 214616 [Multi-domain]  Cd Length: 95  Bit Score: 99.47  E-value: 2.95e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959    177 GEEYVACLPDNSSGTVAAVSFSAAHegLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSA-----SFACLSLCSGp 251
Cdd:smart00321    1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
                            90       100
                    ....*....|....*....|
gi 119605959    252 ppPPAPTCRGPTLLQHVFPA 271
Cdd:smart00321   78 --YPAEVCGGPNRLSVYVLA 95
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
3120-3223 2.84e-23

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 97.50  E-value: 2.84e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3120 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 3198
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
                           90       100
                   ....*....|....*....|....*.
gi 119605959  3199 HVIV-RDLQTARSAFFLVNDWLSVET 3223
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGSK 106
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
3118-3220 1.95e-19

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 86.16  E-value: 1.95e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKglSPAW 3195
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
                            90       100
                    ....*....|....*....|....*
gi 119605959   3196 FLQHVIVRDLQTARSAFFLVNDWLS 3220
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVY 103
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
418-531 1.01e-16

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 78.82  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  418 HCYRLVVEKAAWLQAQEQCQAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGVEVGPAPQGEAFSleSCQNW 495
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119605959  496 LPGEPHPATAEHCVRL--GPTGWCNTDLCSAPHSYVCE 531
Cdd:cd00037    78 APGEPNPGGSEDCVVLssSSDGKWNDVSCSSKLPFICE 115
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1469-1775 1.09e-12

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 72.78  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1469 TSIKVNGSLGLELQqpylFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEV-SRSEAWLNVTVKRR 1547
Cdd:COG3291     2 TATPTSGCAPLTVQ----FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1548 VRGLVVNASRTVVPLNGSVSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVY 1627
Cdd:COG3291    78 NPGVTTVTTSTTVTTLANTANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1628 VLQLIEGLQVVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAW 1707
Cdd:COG3291   157 TSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLT 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1708 ADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPG 1775
Cdd:COG3291   237 GISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTAD 304
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
3011-3060 3.22e-10

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 58.17  E-value: 3.22e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 119605959   3011 YTSLCQYFSEEDMVWRTEGLLPLEETSpRQAVCLTRHLTAFGASLFVPPS 3060
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFAVLMDVPPI 49
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
54-127 6.35e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 59.41  E-value: 6.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959   54 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSALAELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 127
Cdd:cd21340   113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-128 4.83e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.79  E-value: 4.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   48 RVNCSGRGLRTLGPALRIPADATALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPF 127
Cdd:COG4886   117 SLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194

                  .
gi 119605959  128 E 128
Cdd:COG4886   195 T 195
PHA03247 PHA03247
large tegument protein UL36; Provisional
496-791 3.18e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  496 LPGEPHPATAEHCVrlgPTGWCnTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLA-----------QQD 564
Cdd:PHA03247 2555 LPPAAPPAAPDRSV---PPPRP-APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  565 GLSAPHEPVEVMVFPGL------------------RLSREAFLTTAEFGTQELRRPAqLRLQVYRLLSTAGTPENGSEPE 626
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPpperprddpapgrvsrprRARRLGRAAQASSPPQRPRRRA-ARPTVGSLTSLADPPPPPPTPE 2709
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  627 SRsPDNRTQLAPAcMPGGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAPYALWREFLFSVPAGPP----------- 695
Cdd:PHA03247 2710 PA-PHALVSATPL-PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpa 2787
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  696 -AQYSVTLHGQDVLMLPGDLVGLQHDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPHLPAQLEGTWACPACALRLLAA 774
Cdd:PHA03247 2788 vASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
                         330
                  ....*....|....*..
gi 119605959  775 TEQLTVLLGLRPNPGLR 791
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVR 2884
 
Name Accession Description Interval E-value
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
97-2728 0e+00

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 4862.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959    97 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLAWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSGC 176
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   177 GEEYVACLPDNSSGTVAAVS----FSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFACLSLCSGPP 252
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   253 PPPAPTCRGPTLLQHVFPASPGATLVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSAEVDAAGP----AASHRYVLP 328
Cdd:TIGR00864  161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   329 GRYHVTAVLALGAGSALLGTDVQVEAAPAALELVCPSSVQSDESLDLSIQNRGGSGLEAAYSIVALGEEPARAVHPLCPS 408
Cdd:TIGR00864  241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   409 DTEIFPGNGHCYRLVVEKAAWLQAQEQCQAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGVEVGPAPQGEA 486
Cdd:TIGR00864  321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   487 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLAQQDGL 566
Cdd:TIGR00864  401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   567 SAP-HEPVEVMVFPGLRLSREAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLAPACMP 642
Cdd:TIGR00864  481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   643 GGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAP----YALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864  561 GEQWCPFAHICLPLDAPCHPQACANGCSQGHGLPGAArmplYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   719 HDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPH------------------------LPAQLEGTWA----CPACALR 770
Cdd:TIGR00864  641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRAswleCAACAIR 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFDVVSPVAGLRVIYPAPRDGRLYVPTNGSALVLQVD 850
Cdd:TIGR00864  721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   851 SGANATATARWPGGSVSARFENVCPALVA-------TFVPGCPWETNDTLFSVVALPWLSEGEHV----VDVVVENSASR 919
Cdd:TIGR00864  801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTAS 999
Cdd:TIGR00864  881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAM 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1000 NHVSNVTVNYNVTVERMNRMQGLQVSTVPAVLSPNATLALTAGVLVDSAVEVAFLWTFGDGEQALHQFQPPYNESFPVPD 1079
Cdd:TIGR00864  961 NHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1080 PSVAQVLVEHNVMHTYAAPGEYLLTVLASNAFENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLY 1159
Cdd:TIGR00864 1041 PSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1160 TWDFGDGSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDMSLAVEQGAPVVVSAAVQTGD 1239
Cdd:TIGR00864 1121 EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGD 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1240 NITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTG 1319
Cdd:TIGR00864 1201 NITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSG 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1320 NPAHYLFDWTFGDGSSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVTLQPERQFVQLGDEAW 1399
Cdd:TIGR00864 1281 NAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQ 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1400 LVACAWPPFPYRYTWDFGTEEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQEPVLVTSIKVNGSLG- 1478
Cdd:TIGR00864 1361 FQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHGn 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1479 -LELQQPYLFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASR 1557
Cdd:TIGR00864 1441 nLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASL 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1558 TVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQV 1637
Cdd:TIGR00864 1521 TNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQI 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1638 VGG-------------GRYFPTNHTVQLQAVVRDGTNVSYSWTAWRD---RGPALAGSGKGFSLTVLEAGTYHVQLRATN 1701
Cdd:TIGR00864 1601 LGEtaegggggvqeldGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN 1680
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1702 MLGSAWADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTM 1781
Cdd:TIGR00864 1681 LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTM 1760
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1782 TAGNPLGSANATVEVDVQVPVSGLSIRASEPGGS-FVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAG 1860
Cdd:TIGR00864 1761 KAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAG 1840
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1861 TFSIRLNASNAVSWVSATYNLTAEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVL-PGPRFSHS 1939
Cdd:TIGR00864 1841 TFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHS 1920
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1940 FPRVGDHVVSVRGKNHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLV 2019
Cdd:TIGR00864 1921 FPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLV 2000
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2020 ILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALQSGP--CFTNRSAQFEAATSPSPRRVAYHWDFG 2097
Cdd:TIGR00864 2001 IHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFG 2080
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2098 DGSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRD 2177
Cdd:TIGR00864 2081 DGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKD 2160
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2178 CVTYQTEYRWEVYRTASCQRPGRPARVALPG-------------VDVSRPRLVLPRLALPVGHYCFVFVVSFGDTPLTQS 2244
Cdd:TIGR00864 2161 CLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA 2240
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2245 IQANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSTV 2323
Cdd:TIGR00864 2241 ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTL 2320
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2324 TIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRG 2403
Cdd:TIGR00864 2321 GIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRG 2400
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2404 RWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRPPLGGSCRLFPLG- 2482
Cdd:TIGR00864 2401 RWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGe 2480
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2483 -------------AVHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFE 2548
Cdd:TIGR00864 2481 tgqehgdkedevwAIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFE 2560
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2549 VGLAVVVQDQLGAAVVALNRSLAITLPEPNGSATGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYERALDV 2628
Cdd:TIGR00864 2561 VGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDS 2640
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2629 AAEPKHERQHRAQIRKNITETLVSLRVHTVDDIQQIAAALAQCMGPSRELVCRSCLKQTLHKLEAMMLILQAETTAGTVT 2708
Cdd:TIGR00864 2641 AAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVT 2720
                         2730      2740
                   ....*....|....*....|
gi 119605959  2709 PTAIGDSILNITGDLIHLAS 2728
Cdd:TIGR00864 2721 PTAIADNILNIMGDLIHLAS 2740
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
2171-2614 7.84e-133

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 425.76  E-value: 7.84e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2171 AHVDLRDCV-TYQTEYRWEVYRTASC---QRPGRPARVALPGVDvsrprlvLPRLALPVGHYCFVFVVSFGDTP-LTQSI 2245
Cdd:pfam02010    1 ASVELNGCFsAYTIDYLWSVFTVSSNlnlQTISSPKDLVLPQLT-------IPSGTLPYGTYVFTLTVSLSSTPsLAGTD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2246 QANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LN 2314
Cdd:pfam02010   74 IITVTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2315 FGPRGSSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCL 2394
Cdd:pfam02010  154 LLQSTSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2395 NCSSGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRP 2470
Cdd:pfam02010  232 NCSSDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAP 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  2471 PLGGSCRLFPLGAvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FE 2548
Cdd:pfam02010  312 PTGGTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQ 387
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959  2549 VGLAVVVQDQLGAAvVALNRSLAITLPEPNGSatglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2614
Cdd:pfam02010  388 VTVVVVVYDSLGAA-TSVSLTITVTPPSSSDE----LLYFLLGTTSDLSALLQSGDPQQAAQLILA 448
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
3118-3237 8.80e-58

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 196.34  E-value: 8.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAW 3195
Cdd:cd01752     1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119605959 3196 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLAA 3237
Cdd:cd01752    81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3713-3891 5.05e-56

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 194.56  E-value: 5.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3713 AFLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEA--LYPDPPGPRVHTCSAAGGFST 3778
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSscLVHDKFVREINECHAGYSPPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3779 SDY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDNRSRAVFL 3852
Cdd:pfam20519   81 EDRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119605959  3853 ELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3891
Cdd:pfam20519  161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
3892-4113 6.81e-44

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 160.91  E-value: 6.81e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3892 RLSAGLSLPLLT-SVCLLLFAVHFAVAEARTWHREGR------WRVLRLgawarwLLVALTAATALVRLAQLGAADRQWT 3964
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRPsylrsvWNLLDL------AIVILSVVLIVLNIYRDFLADRLIK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3965 rFVRGRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLA 4044
Cdd:pfam08016   75 -SVEASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFG 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959  4045 ILLVSSCVDSLWSVAQALLVLCPgtglsTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4113
Cdd:pfam08016  154 YLLFGTQAPNFSNFVKSILTLFR-----TILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
3118-3237 6.25e-28

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 111.11  E-value: 6.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD---GDRAFHRNSLDIFRIATPhSLGSVWKIRVWHDNKGLSPA 3194
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKksnNKNKFERGQTDKFTVEAV-DLGKLKKIRIGHDNSGLGAG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119605959 3195 WFLQHVIVRDLQTARSAFFLVNDWLSveTEANGGLVEKEVLAA 3237
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLD--KDEDDGQIVRELYPS 120
WSC smart00321
present in yeast cell wall integrity and stress response component proteins; Domain present in ...
177-271 2.95e-24

present in yeast cell wall integrity and stress response component proteins; Domain present in WSC proteins, polycystin and fungal exoglucanase


Pssm-ID: 214616 [Multi-domain]  Cd Length: 95  Bit Score: 99.47  E-value: 2.95e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959    177 GEEYVACLPDNSSGTVAAVSFSAAHegLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSA-----SFACLSLCSGp 251
Cdd:smart00321    1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
                            90       100
                    ....*....|....*....|
gi 119605959    252 ppPPAPTCRGPTLLQHVFPA 271
Cdd:smart00321   78 --YPAEVCGGPNRLSVYVLA 95
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
3120-3223 2.84e-23

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 97.50  E-value: 2.84e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  3120 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 3198
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
                           90       100
                   ....*....|....*....|....*.
gi 119605959  3199 HVIV-RDLQTARSAFFLVNDWLSVET 3223
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGSK 106
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
3118-3220 1.95e-19

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 86.16  E-value: 1.95e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKglSPAW 3195
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
                            90       100
                    ....*....|....*....|....*
gi 119605959   3196 FLQHVIVRDLQTARSAFFLVNDWLS 3220
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVY 103
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1723-1792 1.30e-17

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 79.74  E-value: 1.30e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1723 VAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSANA 1792
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
406-531 1.51e-17

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 81.49  E-value: 1.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959    406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFL---VSRVTRSLDVWIGFSTVQGVEVGPAP 482
Cdd:smart00034    1 CPSGWISY--GGKCYKFSTEKKTWEDAQAFCQS-LGGHLASIHSEAENDFVaslLKNSGSSDYYWIGLSDPDSNGSWQWS 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 119605959    483 QGeaFSLESCQNWLPGEPhPATAEHCVRLGPTGWC-NTDLCSAPHSYVCE 531
Cdd:smart00034   78 DG--SGPVSYSNWAPGEP-NNSSGDCVVLSTSGGKwNDVSCTSKLPFVCE 124
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1128-1209 6.44e-17

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 78.26  E-value: 6.44e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   1128 SVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVR 1207
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTATSSDDGSIVSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVV 77

                    ..
gi 119605959   1208 VF 1209
Cdd:smart00089   78 VQ 79
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
418-531 1.01e-16

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 78.82  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  418 HCYRLVVEKAAWLQAQEQCQAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGVEVGPAPQGEAFSleSCQNW 495
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119605959  496 LPGEPHPATAEHCVRL--GPTGWCNTDLCSAPHSYVCE 531
Cdd:cd00037    78 APGEPNPGGSEDCVVLssSSDGKWNDVSCSSKLPFICE 115
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1892-1961 1.43e-16

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 76.66  E-value: 1.43e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1892 LWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQA 1961
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1637-1708 1.92e-16

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 76.27  E-value: 1.92e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119605959  1637 VVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRdrGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWA 1708
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGD--SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
3119-3220 2.22e-16

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 77.76  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3119 KYEILVKTGWGRGSGTTAHVGIMLYGVD-SRSGHRHLDGDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFL 3197
Cdd:cd00113     2 RYTVTIKTGDKKGAGTDSNISLALYGENgNSSDIPILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWYC 81
                          90       100
                  ....*....|....*....|...
gi 119605959 3198 QHVIVRDLQTARSAFFLVNDWLS 3220
Cdd:cd00113    82 ESITVQALGTKKVYTFPVNRWVL 104
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1553-1622 2.86e-16

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 75.89  E-value: 2.86e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1553 VNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQD 1622
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
2068-2135 3.83e-16

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 75.50  E-value: 3.83e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959  2068 SGPCFTNRSAQFEAaTSPSPRRVAYHWDFGDgSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVA 2135
Cdd:pfam00801    5 GTVVAAGQPVTFTA-TLADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1131-1202 4.66e-16

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 75.50  E-value: 4.66e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119605959  1131 VGVSDGVLVAGRPVTFYPHpLPSPGGVLYTWDFGDgSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAA 1202
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTAT-LADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1385-1456 9.49e-16

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 74.35  E-value: 9.49e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119605959  1385 LQPERQFVQLGDEAWLVACAWPPFPYRYTWDFGteEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAAND 1456
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFG--DSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
2060-2142 2.93e-15

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 73.25  E-value: 2.93e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   2060 AVQYVALQSGPcfTNRSAQFEAATSPSPRRVAYHWDFGDGSpgqDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATV 2139
Cdd:smart00089    2 ADVSASPTVGV--AGESVTFTATSSDDGSIVSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76

                    ...
gi 119605959   2140 TVQ 2142
Cdd:smart00089   77 VVQ 79
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1220-1285 7.43e-15

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 72.03  E-value: 7.43e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959  1220 SLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLAR 1285
Cdd:pfam00801    5 GTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1812-1877 9.39e-15

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 71.65  E-value: 9.39e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959  1812 PGGSFVAAGSSVPFWGQLATGTNVSWCWAVPG--GSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSA 1877
Cdd:pfam00801    3 ASGTVVAAGQPVTFTATLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1129-1203 3.38e-14

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 70.60  E-value: 3.38e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 1129 VAVGVSDGVLV-AGRPVTFYPHPLPSPGGVLYTWDFGDGSpVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQ 1203
Cdd:cd00146     1 PTASVSAPPVAeLGASVTFSASDSSGGSIVSYKWDFGDGE-VSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTK 75
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1550-1628 1.08e-13

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 69.02  E-value: 1.08e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   1550 GLVVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRctPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYV 1628
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTaTSSDDGSIVSYTWDFGDG--TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVV 78
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1468-1545 2.65e-13

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 67.86  E-value: 2.65e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   1468 VTSIKVNGSLGLeLQQPYLFSAV--GRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVK 1545
Cdd:smart00089    1 VADVSASPTVGV-AGESVTFTATssDDGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1469-1775 1.09e-12

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 72.78  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1469 TSIKVNGSLGLELQqpylFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEV-SRSEAWLNVTVKRR 1547
Cdd:COG3291     2 TATPTSGCAPLTVQ----FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1548 VRGLVVNASRTVVPLNGSVSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVY 1627
Cdd:COG3291    78 NPGVTTVTTSTTVTTLANTANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1628 VLQLIEGLQVVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAW 1707
Cdd:COG3291   157 TSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLT 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1708 ADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPG 1775
Cdd:COG3291   237 GISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTAD 304
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1473-1538 2.24e-12

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 64.72  E-value: 2.24e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959  1473 VNGSLGLELQQPYLFSA-VGRGRPASYLWDLGD--GGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEA 1538
Cdd:pfam00801    2 SASGTVVAAGQPVTFTAtLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1725-1799 2.34e-12

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 65.17  E-value: 2.34e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959   1725 ASPNPAAVNTSVTLSAELAG-GSGVVYTWSLEEGLSWetSEPFTTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQ 1799
Cdd:smart00089    6 ASPTVGVAGESVTFTATSSDdGSIVSYTWDFGDGTSS--TGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1819-1878 3.70e-12

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 64.78  E-value: 3.70e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119605959   1819 AGSSVPFWGQLAT-GTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSAT 1878
Cdd:smart00089   13 AGESVTFTATSSDdGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASAT 73
WSC pfam01822
WSC domain; This domain is involved in carbohydrate binding.
180-250 8.00e-12

WSC domain; This domain is involved in carbohydrate binding.


Pssm-ID: 460348  Cd Length: 82  Bit Score: 63.63  E-value: 8.00e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119605959   180 YVACLPDNSsGTVAAVSFSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFA----CLSLCSG 250
Cdd:pfam01822    1 YLGCYSDGT-GGRRLLLGSSGDYDDMTPEKCIAFCSAAGYTYAGLEYGGECYCGNSLPSGSALAdssdCNTPCPG 74
LRR_8 pfam13855
Leucine rich repeat;
70-127 1.21e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.54  E-value: 1.21e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959    70 TALDVSHNLLRALDVGLLANLSALAELDISNNKISTLEEGIFANLFNLSEINLSGNPF 127
Cdd:pfam13855    4 RSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1980-2051 1.79e-11

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 62.40  E-value: 1.79e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119605959  1980 CEPGIATGTERNFTARVQRGSRVAYAWYFslqkvqGDSLV-ILSGRDVTYTPVAAGLLEIQVRAFNALGSENR 2051
Cdd:pfam00801    4 SGTVVAAGQPVTFTATLADGSNVTYTWDF------GDSPGtSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
2073-2143 1.86e-11

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 62.51  E-value: 1.86e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119605959 2073 TNRSAQFEAATSPSPRRVAYHWDFGDGSpGQDTDEPRAEHSYLRPGDYRVQVNASNLVSfFVAQATVTVQV 2143
Cdd:cd00146    13 LGASVTFSASDSSGGSIVSYKWDFGDGE-VSSSGEPTVTHTYTKPGTYTVTLTVTNAVG-SSSTKTTTVVV 81
LRRCT smart00082
Leucine rich repeat C-terminal domain;
125-177 2.41e-11

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 61.29  E-value: 2.41e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 119605959    125 NPFECDCGLAWLPRWAeEQQVRVVQPEAATCAGPGSLAGqPLLGIPLLDSGCG 177
Cdd:smart00082    1 NPFICDCELRWLLRWL-QANEHLQDPVDLRCASPSSLRG-PLLELLHSEFKCP 51
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1552-1628 4.94e-11

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 61.36  E-value: 4.94e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 1552 VVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQ-DSIFVYV 1628
Cdd:cd00146     3 ASVSAPPVAELGASVTFSaSDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
406-531 5.38e-11

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 62.71  E-value: 5.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFLVSRVTRSLDVWIGFStVQGVE-----V-G 479
Cdd:cd03590     1 CPTNWKSF--QSSCYFFSTEKKSWEESRQFCED-MGAHLVIINSQEEQEFISKILSGNRSYWIGLS-DEETEgewkwVdG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959  480 PAPqgeafsLESCQNWLPGEP--HPATAEHCVRLGPT--GWcNTDLCSAPHSYVCE 531
Cdd:cd03590    77 TPL------NSSKTFWHPGEPnnWGGGGEDCAELVYDsgGW-NDVPCNLEYRWICE 125
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
277-344 1.01e-10

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 60.09  E-value: 1.01e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959   277 LVGPHGPLASGQLAAFHIA-APLPVTATRWDFGDgSAEVDAAGPAASHRYVLPGRYHVTAVLALGAGSA 344
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATlADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSA 68
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1296-1377 1.85e-10

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 59.77  E-value: 1.85e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   1296 VLRVEPAACIPTQP-DARLTAYVTGNPAHYLFDWTFGDGssnTTVRGcPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSI 1374
Cdd:smart00089    1 VADVSASPTVGVAGeSVTFTATSSDDGSIVSYTWDFGDG---TSSTG-PTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76

                    ...
gi 119605959   1375 CVE 1377
Cdd:smart00089   77 VVQ 79
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
3011-3060 3.22e-10

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 58.17  E-value: 3.22e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 119605959   3011 YTSLCQYFSEEDMVWRTEGLLPLEETSpRQAVCLTRHLTAFGASLFVPPS 3060
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFAVLMDVPPI 49
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1407-1463 4.51e-10

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 58.62  E-value: 4.51e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959   1407 PFPYRYTWDFGTEeaapTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQ 1463
Cdd:smart00089   27 GSIVSYTWDFGDG----TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1645-1712 3.57e-09

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 56.31  E-value: 3.57e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959   1645 PTNHTVQLQAVVR-DGTNVSYSWtawrDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTM 1712
Cdd:smart00089   12 VAGESVTFTATSSdDGSIVSYTW----DFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1222-1281 4.95e-09

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 55.97  E-value: 4.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119605959 1222 AVEQGAPVVVSAAVQ-TGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAG 1281
Cdd:cd00146    10 VAELGASVTFSASDSsGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVG 70
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
54-127 6.35e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 59.41  E-value: 6.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959   54 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSALAELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 127
Cdd:cd21340   113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
406-531 7.35e-09

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 57.00  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  406 CPSDTeiFPGNGHCYRLVVEKAAWLQAQEQCQAW-AGAALAMVDSPAVQRFLVSRV----TRSLDVWIGFSTVQGVEVGP 480
Cdd:cd03594     1 CPKGW--LPYKGNCYGYFRQPLSWSDAELFCQKYgPGAHLASIHSPAEAAAIASLIssyqKAYQPVWIGLHDPQQSRGWE 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119605959  481 APQGEAFSLEScqnWLPGEPHPaTAEHCVRL-GPTG---WcNTDLCSAPHSYVCE 531
Cdd:cd03594    79 WSDGSKLDYRS---WDRNPPYA-RGGYCAELsRSTGflkW-NDANCEERNPFICK 128
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1226-1292 8.28e-09

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 55.15  E-value: 8.28e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959   1226 GAPVVVSAAVQT-GDNITWTFDMGDGTVLSGPeaTVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVF 1292
Cdd:smart00089   14 GESVTFTATSSDdGSIVSYTWDFGDGTSSTGP--TVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
70-128 1.67e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.33  E-value: 1.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959   70 TALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEgiFANLFNLSEINLSGNPFE 128
Cdd:COG4886   208 EELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLT 263
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1140-1350 2.29e-08

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 59.30  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1140 AGRPVTFYPHplpSPGGVL-YTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTV-SGAAAQADVRVFEELRGLSV 1217
Cdd:COG3291    10 APLTVQFTDT---SSGNATsYEWDFGDGT---TSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1218 DMSLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVL 1297
Cdd:COG3291    84 VTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTD 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119605959 1298 RVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCPTVTHNFT 1350
Cdd:COG3291   164 VTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATS 216
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1480-1544 2.79e-08

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 53.65  E-value: 2.79e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1480 ELQQPYLFSAV--GRGRPASYLWDLGDGGWL--EGPEVTHAYNSTGDFTVRVAGWNEVSRSEA-WLNVTV 1544
Cdd:cd00146    12 ELGASVTFSASdsSGGSIVSYKWDFGDGEVSssGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTkTTTVVV 81
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1807-1878 3.33e-08

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 53.27  E-value: 3.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 1807 IRASEPGGSFVAAGSSVPFWGQLATG---TNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSAT 1878
Cdd:cd00146     1 PTASVSAPPVAELGASVTFSASDSSGgsiVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTK 75
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1024-1116 4.17e-08

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 52.77  E-value: 4.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1024 VSTVPAVLSPNATLALTAGVLvdSAVEVAFLWTFGDgeqalhqfqppynesfpvpdpSVAQVLVEHNVMHTYAAPGEYLL 1103
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLA--DGSNVTYTWDFGD---------------------SPGTSGSGPTVTHTYLSPGTYTV 57
                           90
                   ....*....|...
gi 119605959  1104 TVLASNAFENLTQ 1116
Cdd:pfam00801   58 TLTASNAVGSANA 70
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-128 4.83e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.79  E-value: 4.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   48 RVNCSGRGLRTLGPALRIPADATALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPF 127
Cdd:COG4886   117 SLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194

                  .
gi 119605959  128 E 128
Cdd:COG4886   195 T 195
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-128 5.00e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.79  E-value: 5.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   48 RVNCSGRGLRTLGPALripADATAL---DVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSG 124
Cdd:COG4886   140 ELDLSNNQLTDLPEPL---GNLTNLkslDLSNNQLTDLPEEL-GNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSG 214

                  ....
gi 119605959  125 NPFE 128
Cdd:COG4886   215 NQLT 218
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1723-1796 7.49e-08

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 52.50  E-value: 7.49e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 1723 VAASPNPAA-VNTSVTLSAE-LAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSAN---ATVEV 1796
Cdd:cd00146     3 ASVSAPPVAeLGASVTFSASdSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSStktTTVVV 81
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1021-1122 8.65e-08

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 52.07  E-value: 8.65e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   1021 GLQVSTVPAVLSPNATLALTAGVLVDSAVeVAFLWTFGDGeqalhqfqppynesfpvpdpsvaQVLVEHNVMHTYAAPGE 1100
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTATSSDDGSI-VSYTWDFGDG-----------------------TSSTGPTVTHTYTKPGT 56
                            90       100
                    ....*....|....*....|..
gi 119605959   1101 YLLTVLASNAFENLTQQVPVSV 1122
Cdd:smart00089   57 YTVTLTVTNAVGSASATVTVVV 78
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
70-128 8.95e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.02  E-value: 8.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959   70 TALDVSHNLLRALDVglLANLSALAELDISNNKISTLEEgiFANLFNLSEINLSGNPFE 128
Cdd:COG4886   231 ETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLT 285
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-128 1.18e-07

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.64  E-value: 1.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959   72 LDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPFE 128
Cdd:COG4886   187 LDLSNNQITDLPEPL-GNLTNLEELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQLT 241
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
3120-3227 1.53e-07

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238852  Cd Length: 129  Bit Score: 52.93  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3120 YEILVKTGWGRGSGTTAHVGIMLYGVDSRS---------GHRHLDGDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKG 3190
Cdd:cd01754     3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGlrianleawGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119605959 3191 LSPAWFLQHVIVRDL-QTARSA--FFLVNDWLSVETEANG 3227
Cdd:cd01754    83 NHPGWYVNYVEVTQAgQHAPCMqhLFAVEQWLATDESPYM 122
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1152-1208 1.86e-07

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 51.50  E-value: 1.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959  1152 PSPGGVL-YTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRV 1208
Cdd:pfam18911   29 DPDGDILsYRWDFGDGT---TATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1307-1380 2.24e-07

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 50.96  E-value: 2.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119605959 1307 TQPDARLTAYVTGNPAHYLFDWTFGDGssNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAhyfTSICVEPEV 1380
Cdd:cd00146    13 LGASVTFSASDSSGGSIVSYKWDFGDG--EVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSS---STKTTTVVV 81
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1304-1369 2.63e-07

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 50.46  E-value: 2.63e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959  1304 CIPTQPDARLTAYV-TGNPAHYLfdWTFGDgsSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAH 1369
Cdd:pfam00801    7 VVAAGQPVTFTATLaDGSNVTYT--WDFGD--SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1888-1967 3.37e-07

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 50.53  E-value: 3.37e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   1888 VGLVLWASSKVVApGQLVHFQI-LLAAGSAVTFRLQVGgaNPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIV 1966
Cdd:smart00089    1 VADVSASPTVGVA-GESVTFTAtSSDDGSIVSYTWDFG--DGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVV 77

                    .
gi 119605959   1967 V 1967
Cdd:smart00089   78 V 78
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1409-1462 8.80e-07

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 49.42  E-value: 8.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 1409 PYRYTWDFGTEEAAPTRarGPEVTFIYRDPGSYLVTVTASNNISAAN-DSALVEV 1462
Cdd:cd00146    29 IVSYKWDFGDGEVSSSG--EPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1725-1902 1.92e-06

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 53.14  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1725 ASPNPAAVNTSVTLSAeLAGGSGVVYTWSLEEGLSweTSEPFTTHSFPTPGLHLVTMTAGNPLGSANA-----TVEVDVQ 1799
Cdd:COG3291     3 ATPTSGCAPLTVQFTD-TSSGNATSYEWDFGDGTT--STEANPSHTYTTPGTYTVTLTVTDAAGCSDTttktiTVGAPNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1800 VPVSGLSIRASEPGGSFVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSATY 1879
Cdd:COG3291    80 GVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSV 159
                         170       180
                  ....*....|....*....|...
gi 119605959 1880 NLTAEEPIVGLVLWASSKVVAPG 1902
Cdd:COG3291   160 STTDVTSDGTTSASTNPSVTTDT 182
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1487-1527 2.41e-06

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 48.42  E-value: 2.41e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 119605959  1487 FSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRV 1527
Cdd:pfam18911   26 ASDDPDGDILSYRWDFGDGTTATGANVSHTYAAPGTYTVTL 66
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1408-1709 4.24e-06

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 52.36  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1408 FPYRYTWDFGTeeaaPTRARGPEVTFIYRDPGSYLVTVTASNNI-SAANDSALVEVQEPVLVTSIKVNGSlglelqqpYL 1486
Cdd:COG3291    23 NATSYEWDFGD----GTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTST--------TV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1487 FSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASRTVVPLNGSV 1566
Cdd:COG3291    91 TTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1567 SFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQVVGGGRYFPT 1646
Cdd:COG3291   171 SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNT 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119605959 1647 NHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWAD 1709
Cdd:COG3291   251 VTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLA 313
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
276-348 5.32e-06

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 47.11  E-value: 5.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959  276 TLVGPHGPLAS-GQLAAFHIAAPLP--VTATRWDFGDGSAEVdAAGPAASHRYVLPGRYHVTAVLALGAGSALLGT 348
Cdd:cd00146     2 TASVSAPPVAElGASVTFSASDSSGgsIVSYKWDFGDGEVSS-SGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKT 76
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1025-1384 1.72e-05

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 50.44  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1025 STVPAVLSPNATLALTAgvlVDSAVEVAFLWTFGDGEQAlhqfqppynesfpvpdpsvaqvlVEHNVMHTYAAPGEYLLT 1104
Cdd:COG3291     2 TATPTSGCAPLTVQFTD---TSSGNATSYEWDFGDGTTS-----------------------TEANPSHTYTTPGTYTVT 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1105 VLASNAF-ENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSPVLTQSQPAANHTYAS 1183
Cdd:COG3291    56 LTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTT 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1184 RGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDmslaveqGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHV 1263
Cdd:COG3291   136 TGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT-------SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1264 YLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCP 1343
Cdd:COG3291   209 GVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGL 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 119605959 1344 TVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVT 1384
Cdd:COG3291   289 GTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSST 329
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
300-344 2.24e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 45.34  E-value: 2.24e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 119605959   300 VTATRWDFGDGSAevdAAGPAASHRYVLPGRYHVTAVLALGAGSA 344
Cdd:pfam18911   34 ILSYRWDFGDGTT---ATGANVSHTYAAPGTYTVTLTVTDDSGAS 75
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
70-128 2.34e-05

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.32  E-value: 2.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959   70 TALDVSHNLLraldvglLANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPFE 128
Cdd:COG4886    99 TELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEEL-ANLTNLKELDLSNNQLT 149
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1411-1462 2.37e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 45.34  E-value: 2.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 119605959  1411 RYTWDFGTEeaapTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEV 1462
Cdd:pfam18911   36 SYRWDFGDG----TTATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1972-2058 2.59e-05

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 45.13  E-value: 2.59e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959   1972 SGLQVPNCCEPgiATGTERNFTARVQR-GSRVAYAWYFslqkvqGDSLViLSGRDVTYTPVAAGLLEIQVRAFNALGSEN 2050
Cdd:smart00089    1 VADVSASPTVG--VAGESVTFTATSSDdGSIVSYTWDF------GDGTS-STGPTVTHTYTKPGTYTVTLTVTNAVGSAS 71

                    ....*...
gi 119605959   2051 RTLVLEVQ 2058
Cdd:smart00089   72 ATVTVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
301-353 2.62e-05

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 45.13  E-value: 2.62e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 119605959    301 TATRWDFGDGSaevDAAGPAASHRYVLPGRYHVTAVLALGAGSALLGTDVQVE 353
Cdd:smart00089   30 VSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1891-1967 3.70e-05

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 44.79  E-value: 3.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1891 VLWASSKVVAPGQLVHFQI-LLAAGSAVTFRLQVGGANPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIVV 1967
Cdd:cd00146     3 ASVSAPPVAELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVV 80
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
2076-2142 4.24e-05

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 48.90  E-value: 4.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 2076 SAQFEAATSPSPrrVAYHWDFGDGSpgqDTDEPRAEHSYLRPGDYRVQVNASNLV-SFFVAQATVTVQ 2142
Cdd:COG3291    13 TVQFTDTSSGNA--TSYEWDFGDGT---TSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVG 75
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
406-531 5.07e-05

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 45.40  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFLvSRVTRSLDVWIGFSTVQGVEVGPAPQGE 485
Cdd:cd03593     1 CPKDWICY--GNKCYYFSMEKKTWNESKEACSS-KNSSLLKIDDEEELEFL-QSQIGSSSYWIGLSREKSEKPWKWIDGS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 119605959  486 AFSlescqNWLpgEPHPATAE-HCVRLGPTGwCNTDLCSAPHSYVCE 531
Cdd:cd03593    77 PLN-----NLF--NIRGSTKSgNCAYLSSTG-IYSEDCSTKKRWICE 115
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
2076-2128 8.30e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 43.80  E-value: 8.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 119605959  2076 SAQFEAATS--PSPRRVAYHWDFGDGSPGqdtDEPRAEHSYLRPGDYRVQVNASN 2128
Cdd:pfam18911   19 TVTFDASASddPDGDILSYRWDFGDGTTA---TGANVSHTYAAPGTYTVTLTVTD 70
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
406-532 1.42e-04

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 44.66  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAWAG----AALAMVDSPAVQRFL------VSRVTRSLDVWIGFStvQG 475
Cdd:cd03589     1 CPTFWTAF--GGYCYRFFGDRLTWEEAELRCRSFSIpgliAHLVSIHSQEENDFVydlfesSRGPDTPYGLWIGLH--DR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119605959  476 VEVGPA--PQGEAFSLEscqNWLPGEPHPA-TAEHCVRLGPTG-----WcNTDLCSAPHSYVCEL 532
Cdd:cd03589    77 TSEGPFewTDGSPVDFT---KWAGGQPDNYgGNEDCVQMWRRGdagqsW-NDMPCDAVFPYICKM 137
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3756-4281 1.42e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 48.33  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3756 EALYPDPPGPRV--------HTCSAAGGFSTSDYDVGWESPHNGSGTWAYSAPDLLGAWSWGSCAVYDSGGYVQELGLSL 3827
Cdd:COG3321   850 SALYPGRGRRRVplptypfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAAL 929
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3828 EESRDRLRFLQLHNWLDNRSRAVFLELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALRRLSAGLSLPLLTSVCL 3907
Cdd:COG3321   930 LALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAA 1009
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3908 LLFAVHFAVAEARTWHREGRWRVLRLGAWARWLLVALTAATALVRLAQLGAADRQWTRFVRGRPRRFTSFDQVAQLSSAA 3987
Cdd:COG3321  1010 LLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAA 1089
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3988 RGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLAILLVSSCVDSLWSVAQALLVLCP 4067
Cdd:COG3321  1090 LAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLA 1169
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 4068 GTGLSTLCPAESWHLSPLLCVGLWALRLWGALRLGAVILRWRYHALRGELYRPAWEPQDYEMVELFLRRLRLWMGLSKVK 4147
Cdd:COG3321  1170 AAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALA 1249
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 4148 EFRHKVRFEGMEPLPSRSSRGSKVSPDVPPPSAGSDASHPSTSSSQLDGLSVSLGRLGTRCEPEPSRLQAVFEALLTQFD 4227
Cdd:COG3321  1250 AAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAA 1329
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 4228 RLNQA-TEDVYQLEQQLHSLQGRRSSRAPAGSSRGPSPGLRPALPSRLARASRGV 4281
Cdd:COG3321  1330 LAALAaAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
PHA03247 PHA03247
large tegument protein UL36; Provisional
496-791 3.18e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  496 LPGEPHPATAEHCVrlgPTGWCnTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLA-----------QQD 564
Cdd:PHA03247 2555 LPPAAPPAAPDRSV---PPPRP-APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  565 GLSAPHEPVEVMVFPGL------------------RLSREAFLTTAEFGTQELRRPAqLRLQVYRLLSTAGTPENGSEPE 626
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPpperprddpapgrvsrprRARRLGRAAQASSPPQRPRRRA-ARPTVGSLTSLADPPPPPPTPE 2709
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  627 SRsPDNRTQLAPAcMPGGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAPYALWREFLFSVPAGPP----------- 695
Cdd:PHA03247 2710 PA-PHALVSATPL-PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpa 2787
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  696 -AQYSVTLHGQDVLMLPGDLVGLQHDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPHLPAQLEGTWACPACALRLLAA 774
Cdd:PHA03247 2788 vASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
                         330
                  ....*....|....*..
gi 119605959  775 TEQLTVLLGLRPNPGLR 791
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVR 2884
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
934-1014 5.62e-04

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 41.28  E-value: 5.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959    934 GLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFnvIYQSAAVFKLSLTASNHVSNVTVNYNVTV 1013
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTATSSDDGSIVSYTWDFGDGTSSTGPTVTH--TYTKPGTYTVTLTVTNAVGSASATVTVVV 78

                    .
gi 119605959   1014 E 1014
Cdd:smart00089   79 Q 79
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1643-1715 6.39e-04

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 41.33  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1643 YFPTNHTVQLQAVVR-------DGTNVSYSWTaWRDrGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTMDFV 1715
Cdd:cd00146     4 SVSAPPVAELGASVTfsasdssGGSIVSYKWD-FGD-GEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
LRR_8 pfam13855
Leucine rich repeat;
93-125 1.24e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.82  E-value: 1.24e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 119605959    93 LAELDISNNKISTLEEGIFANLFNLSEINLSGN 125
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNN 35
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1723-1800 2.22e-03

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 39.95  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959  1723 VAASPNPAAVNTSVTLSAE---LAGGSGVVYTWSLEEGLSWETSEPftTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQ 1799
Cdd:pfam18911    7 DAGGDRIVAEGETVTFDASasdDPDGDILSYRWDFGDGTTATGANV--SHTYAAPGTYTVTLTVTDDSGASNSTATDTVT 84

                   .
gi 119605959  1800 V 1800
Cdd:pfam18911   85 V 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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